ID A0A6P6N9H9_CARAU Unreviewed; 495 AA.
AC A0A6P6N9H9;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 18-JUN-2025, entry version 22.
DE RecName: Full=DNA-directed DNA/RNA polymerase mu {ECO:0000256|PIRNR:PIRNR000817};
DE EC=2.7.7.7 {ECO:0000256|PIRNR:PIRNR000817};
GN Name=LOC113077836 {ECO:0000313|RefSeq:XP_026105885.1};
OS Carassius auratus (Goldfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Carassius.
OX NCBI_TaxID=7957 {ECO:0000313|Proteomes:UP000515129, ECO:0000313|RefSeq:XP_026105885.1};
RN [1] {ECO:0000313|RefSeq:XP_026105885.1}
RP IDENTIFICATION.
RC STRAIN=Wakin {ECO:0000313|RefSeq:XP_026105885.1};
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_026105885.1};
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- FUNCTION: Gap-filling polymerase involved in repair of DNA double-
CC strand breaks by non-homologous end joining (NHEJ).
CC {ECO:0000256|PIRNR:PIRNR000817}.
CC -!- FUNCTION: Template-independent DNA polymerase which catalyzes the
CC random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a
CC DNA initiator. One of the in vivo functions of this enzyme is the
CC addition of nucleotides at the junction (N region) of rearranged Ig
CC heavy chain and T-cell receptor gene segments during the maturation of
CC B- and T-cells. {ECO:0000256|ARBA:ARBA00037135}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) +
CC diphosphate; Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-
CC COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112;
CC EC=2.7.7.31; Evidence={ECO:0000256|ARBA:ARBA00048976};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) +
CC diphosphate; Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-
CC COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112;
CC EC=2.7.7.7; Evidence={ECO:0000256|PIRNR:PIRNR000817};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR000817, ECO:0000256|PIRSR:PIRSR000817-1};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR000817}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family.
CC {ECO:0000256|ARBA:ARBA00008323, ECO:0000256|PIRNR:PIRNR000817}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_026105885.1; XM_026250100.1.
DR AlphaFoldDB; A0A6P6N9H9; -.
DR SMR; A0A6P6N9H9; -.
DR GeneID; 113077836; -.
DR KEGG; caua:113077836; -.
DR OrthoDB; 205514at2759; -.
DR Proteomes; UP000515129; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003912; F:DNA nucleotidylexotransferase activity; IEA:TreeGrafter.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:TreeGrafter.
DR CDD; cd17713; BRCT_polymerase_mu_like; 1.
DR CDD; cd00141; NT_POLXc; 1.
DR FunFam; 3.30.210.10:FF:000003; DNA nucleotidylexotransferase; 1.
DR FunFam; 1.10.150.20:FF:000010; DNA polymerase lambda; 1.
DR FunFam; 1.10.150.110:FF:000003; DNA polymerase mu; 1.
DR FunFam; 3.40.50.10190:FF:000035; DNA-directed DNA/RNA polymerase mu; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 1.10.150.110; DNA polymerase beta, N-terminal domain-like; 1.
DR Gene3D; 3.30.210.10; DNA polymerase, thumb domain; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR002054; DNA-dir_DNA_pol_X.
DR InterPro; IPR027249; DNA/RNApol_mu.
DR InterPro; IPR019843; DNA_pol-X_BS.
DR InterPro; IPR010996; DNA_pol_b-like_N.
DR InterPro; IPR028207; DNA_pol_B_palm_palm.
DR InterPro; IPR018944; DNA_pol_lambd_fingers_domain.
DR InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
DR InterPro; IPR037160; DNA_Pol_thumb_sf.
DR InterPro; IPR022312; DNA_pol_X.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR029398; PolB_thumb.
DR InterPro; IPR001726; TdT/Mu.
DR PANTHER; PTHR11276:SF21; DNA NUCLEOTIDYLEXOTRANSFERASE; 1.
DR PANTHER; PTHR11276; DNA POLYMERASE TYPE-X FAMILY MEMBER; 1.
DR Pfam; PF14792; DNA_pol_B_palm; 1.
DR Pfam; PF14791; DNA_pol_B_thumb; 1.
DR Pfam; PF10391; DNA_pol_lambd_f; 1.
DR Pfam; PF14716; HHH_8; 1.
DR PIRSF; PIRSF000817; DNA_NT; 1.
DR PIRSF; PIRSF501176; DNApol_mu; 1.
DR PRINTS; PR00869; DNAPOLX.
DR PRINTS; PR00871; DNAPOLXTDT.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00483; POLXc; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF47802; DNA polymerase beta, N-terminal domain-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81585; PsbU/PolX domain-like; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS00522; DNA_POLYMERASE_X; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000817};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000817};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|PIRNR:PIRNR000817};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR000817};
KW Reference proteome {ECO:0000313|Proteomes:UP000515129};
KW Terminal addition {ECO:0000256|ARBA:ARBA00022639};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000817}.
FT DOMAIN 22..119
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 122..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 334
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000817-1"
FT BINDING 336
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000817-1"
FT BINDING 419
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000817-1"
SQ SEQUENCE 495 AA; 56509 MW; F4D7D683B2B2B867 CRC64;
MFPKALPTRK RRRTEVASVG GRDEVKFRDV TLFLVEKRMG KSRRNFLSNL ARSKGFCLDD
ALSADVTHVV SEGNAAQELW SWLEEQGFRE MQDKHVLHIS WFTESMSAGR PVPPEIRHYI
QNPAVDQRSR TNPSAKPESA LSPYACQRRT TMDNHNKIFT DALEVLAENL ELGGNQGPSL
AFRRAASVLK SLPAALRHLQ ETQHLPCLGE HSRAIIEEIF EYGSSSRVEE ILNDERYRTM
KLFSSVFGVG PKTSESWFCR GLRSFEQVLS EPSVRLNRMQ TAGFLFYEDI SKPVSRTEAS
ALKIIVEEAV ISVNPSATVS ITGGFRRGKE FGHDVDFIIK TPEAGQEDVI LTAVIERFKS
QNILLYSDFQ ESTFDLRQLP THCFEAMDHY SKCFLIIKLK REQETDARAG RDWRAVRVDL
VAPPLERFAY ALLGWTGSTL FERDLRRFAR LERGKLLDNH TLYDKATNTF LPANTEEDIF
AHLGLEYIEP WQRNA
//
